8HUC

Crystal structure of PaIch (Pec1)

8HUC の概要

• エントリーDOI: 10.2210/pdb8huc/pdb
• 分子名称: MaoC_dehydrat_N domain-containing protein, GLYCEROL, NITRATE ION, ... (4 entities in total)
• 機能のキーワード: hydro-lyase., unknown function
• 由来する生物種: Pseudomonas aeruginosa UCBPP-PA14
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 123826.46

構造登録者

Pramanik, A.,Datta, S. (登録日: 2022-12-23, 公開日: 2023-12-27, 最終更新日: 2024-06-26)

主引用文献

Pramanik, A.,Datta, S.
Structural and functional insights of itaconyl-CoA hydratase from Pseudomonas aeruginosa highlight a novel N-terminal hotdog fold.
Febs Lett., 598:1387-1401, 2024

PubMed Abstract: Itaconyl-CoA hydratase in Pseudomonas aeruginosa (PaIch) converts itaconyl-CoA to (S)-citramalyl-CoA upon addition of a water molecule, a part of an itaconate catabolic pathway in virulent organisms required for their survival in humans host cells. Crystal structure analysis of PaIch showed that a unique N-terminal hotdog fold containing a 4-residue short helical segment α3-, named as an "eaten sausage", followed by a flexible loop region slipped away from the conserved β-sheet scaffold, whereas the C-terminal hotdog fold is similar to all MaoC. A conserved hydratase motif with catalytic residues provides mechanistic insights into catalysis, and existence of a longer substrate binding tunnel may suggest the binding of longer CoA derivatives.

PubMed: 38575551
DOI: 10.1002/1873-3468.14867

実験手法

X-RAY DIFFRACTION (1.984 Å)